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Structure and immunogenicity of a stabilized HIV-1 envelope trimer based on a group-M consensus sequence.

Publication ,  Journal Article
Sliepen, K; Han, BW; Bontjer, I; Mooij, P; Garces, F; Behrens, A-J; Rantalainen, K; Kumar, S; Sarkar, A; Brouwer, PJM; Hua, Y; Tolazzi, M ...
Published in: Nat Commun
May 29, 2019

Stabilized HIV-1 envelope glycoproteins (Env) that resemble the native Env are utilized in vaccination strategies aimed at inducing broadly neutralizing antibodies (bNAbs). To limit the exposure of rare isolate-specific antigenic residues/determinants we generated a SOSIP trimer based on a consensus sequence of all HIV-1 group M isolates (ConM). The ConM trimer displays the epitopes of most known bNAbs and several germline bNAb precursors. The crystal structure of the ConM trimer at 3.9 Å resolution resembles that of the native Env trimer and its antigenic surface displays few rare residues. The ConM trimer elicits strong NAb responses against the autologous virus in rabbits and macaques that are significantly enhanced when it is presented on ferritin nanoparticles. The dominant NAb specificity is directed against an epitope at or close to the trimer apex. Immunogens based on consensus sequences might have utility in engineering vaccines against HIV-1 and other viruses.

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Published In

Nat Commun

DOI

EISSN

2041-1723

Publication Date

May 29, 2019

Volume

10

Issue

1

Start / End Page

2355

Location

England

Related Subject Headings

  • env Gene Products, Human Immunodeficiency Virus
  • Rabbits
  • Protein Multimerization
  • Macaca
  • HIV-1
  • HIV Antibodies
  • Epitopes
  • Consensus Sequence
  • Antibodies, Neutralizing
  • Animals
 

Citation

APA
Chicago
ICMJE
MLA
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Sliepen, K., Han, B. W., Bontjer, I., Mooij, P., Garces, F., Behrens, A.-J., … Sanders, R. W. (2019). Structure and immunogenicity of a stabilized HIV-1 envelope trimer based on a group-M consensus sequence. Nat Commun, 10(1), 2355. https://doi.org/10.1038/s41467-019-10262-5
Sliepen, Kwinten, Byung Woo Han, Ilja Bontjer, Petra Mooij, Fernando Garces, Anna-Janina Behrens, Kimmo Rantalainen, et al. “Structure and immunogenicity of a stabilized HIV-1 envelope trimer based on a group-M consensus sequence.Nat Commun 10, no. 1 (May 29, 2019): 2355. https://doi.org/10.1038/s41467-019-10262-5.
Sliepen K, Han BW, Bontjer I, Mooij P, Garces F, Behrens A-J, et al. Structure and immunogenicity of a stabilized HIV-1 envelope trimer based on a group-M consensus sequence. Nat Commun. 2019 May 29;10(1):2355.
Sliepen, Kwinten, et al. “Structure and immunogenicity of a stabilized HIV-1 envelope trimer based on a group-M consensus sequence.Nat Commun, vol. 10, no. 1, May 2019, p. 2355. Pubmed, doi:10.1038/s41467-019-10262-5.
Sliepen K, Han BW, Bontjer I, Mooij P, Garces F, Behrens A-J, Rantalainen K, Kumar S, Sarkar A, Brouwer PJM, Hua Y, Tolazzi M, Schermer E, Torres JL, Ozorowski G, van der Woude P, de la Peña AT, van Breemen MJ, Camacho-Sánchez JM, Burger JA, Medina-Ramírez M, González N, Alcami J, LaBranche C, Scarlatti G, van Gils MJ, Crispin M, Montefiori DC, Ward AB, Koopman G, Moore JP, Shattock RJ, Bogers WM, Wilson IA, Sanders RW. Structure and immunogenicity of a stabilized HIV-1 envelope trimer based on a group-M consensus sequence. Nat Commun. 2019 May 29;10(1):2355.

Published In

Nat Commun

DOI

EISSN

2041-1723

Publication Date

May 29, 2019

Volume

10

Issue

1

Start / End Page

2355

Location

England

Related Subject Headings

  • env Gene Products, Human Immunodeficiency Virus
  • Rabbits
  • Protein Multimerization
  • Macaca
  • HIV-1
  • HIV Antibodies
  • Epitopes
  • Consensus Sequence
  • Antibodies, Neutralizing
  • Animals